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001     283048
005     20260217130612.0
024 7 _ |2 doi
|a 10.1073/pnas.2513375122
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|a pmid:41428877
024 7 _ |2 ISSN
|a 0027-8424
024 7 _ |2 ISSN
|a 1091-6490
037 _ _ |a DZNE-2025-01455
041 _ _ |a English
082 _ _ |a 500
100 1 _ |0 0000-0001-7368-5539
|a Vierock, Johannes
|b 0
245 _ _ |a Multicolor photoreactions of the red light-activated channelrhodopsin Chrimson.
260 _ _ |a Washington, DC
|b National Acad. of Sciences
|c 2025
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520 _ _ |a Channelrhodopsins are light-gated ion channels that are used in modern neurosciences for the precise control of cellular ion fluxes by light. With a peak absorption at 585 nm, Chrimson is the most red-shifted cation-conducting ChR. It is frequently employed in multicolor experiments alongside blue light-sensitive optogenetic tools and is so far the only light-gated ion channel successfully applied in human vision restoration. However, its photoresponses to different wavelengths have not been thoroughly characterized. In this study, we identify multiple interconvertible dark states of Chrimson with distinct absorption and photokinetic properties. Combining electrophysiology and spectroscopy with optogenetic experiments in neurons, we unveil that this dark state heterogeneity is based on distinct protonation dynamics of the counterion complex and alternative retinal isomerization. In neurons, prolonged red illumination reduces Chrimson's red light sensitivity, which is reflected by a blue shift of the action spectrum. Blue light pulses reverse this shift and increase the excitability in subsequent red-light flashes. This understanding of wavelength-dependent photoreactions in Chrimson will improve the design of multicolor optogenetic experiments and inform strategies for optimizing Chrimson for therapeutic applications.
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650 _ 7 |2 Other
|a Chrimson
650 _ 7 |2 Other
|a FTIR spectroscopy
650 _ 7 |2 Other
|a channelrhodopsins
650 _ 7 |2 Other
|a optogenetics
650 _ 7 |2 Other
|a retinal prosthesis
650 _ 7 |2 NLM Chemicals
|a Channelrhodopsins
650 _ 2 |2 MeSH
|a Channelrhodopsins: metabolism
650 _ 2 |2 MeSH
|a Channelrhodopsins: chemistry
650 _ 2 |2 MeSH
|a Channelrhodopsins: genetics
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Optogenetics: methods
650 _ 2 |2 MeSH
|a Neurons: metabolism
650 _ 2 |2 MeSH
|a Neurons: radiation effects
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a HEK293 Cells
650 _ 2 |2 MeSH
|a Red Light
700 1 _ |a Kaufmann, Joel C D
|b 1
700 1 _ |0 P:(DE-2719)9001061
|a Faiß, Lukas
|b 2
|e First author
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700 1 _ |a Tillert, Linda
|b 3
700 1 _ |a Krause, Benjamin S
|b 4
700 1 _ |a Fischer, Paul
|b 5
700 1 _ |a Nguyen, Thi Bich Thao
|b 6
700 1 _ |0 P:(DE-2719)2810725
|a Schmitz, Dietmar
|b 7
700 1 _ |0 P:(DE-2719)2810914
|a Rost, Benjamin R
|b 8
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700 1 _ |a Bartl, Franz
|b 9
700 1 _ |0 0000-0003-3589-6452
|a Hegemann, Peter
|b 10
773 _ _ |0 PERI:(DE-600)1461794-8
|a 10.1073/pnas.2513375122
|g Vol. 122, no. 52, p. e2513375122
|n 52
|p e2513375122
|t Proceedings of the National Academy of Sciences of the United States of America
|v 122
|x 0027-8424
|y 2025
856 4 _ |u https://pub.dzne.de/record/283048/files/DZNE-2025-1455.pdf
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